| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10797327 | Biochimica et Biophysica Acta (BBA) - Biomembranes | 2012 | 8 Pages |
Abstract
⺠The intact purified FsrC membrane histidine kinase was studied by SRCD spectroscopy. ⺠Far-UV spectra revealed that FsrC is 61% α-helical and relatively thermostable. ⺠Tertiary structure was found to be significantly affected upon GBAP ligand binding. ⺠Titration experiments revealed a calculated kd value of 2 μM. ⺠SRCD provides a valuable screening tool for membrane protein stability under a range of detergent conditions.
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Authors
Simon G. Patching, Shalini Edara, Pikyee Ma, Jiro Nakayama, Rohanah Hussain, Giuliano Siligardi, Mary K. Phillips-Jones,